Premium
Cover Feature: Hidden Specificities in Enzyme Catalysis: Structural Basis of Substrate Structure‐Selectivity Relationship of a Ketoreductase (ChemBioChem 9/2019)
Author(s) -
Häckh Matthias,
Lucas Xavier,
Marolt Marija,
Leadlay Peter F.,
Müller Michael,
Günther Stefan,
Lüdeke Steffen
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900222
Subject(s) - moiety , stereoselectivity , stereochemistry , chemistry , cover (algebra) , substrate (aquarium) , selectivity , enzyme , feature (linguistics) , catalysis , biochemistry , biology , philosophy , ecology , linguistics , mechanical engineering , engineering
The cover feature picture shows a two‐faced clown twisting balloons into different shapes depending on which type of balloon he grabs. Similarly, the ketoreductase Tyl‐KR1 converts methylated keto esters diastereoselectively into either R , R ‐ or S , S ‐configured hydroxyesters, depending simply on the choice of ester moiety. In their communication, S. Lüdeke et al. on page 1150 in Issue 9, 2019 (DOI: 10.1002/cbic.201800799) unravel a relationship between substrate structure and the stereoselectivity of the reaction, identifying two binding modes, one being R , R ‐ and the other being S , S ‐specific. Interestingly, it is not size that matters, but subtle electrostatic interactions that exist in one, but not in the other mode.